MIPT3_MOUSE - dbPTM
MIPT3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MIPT3_MOUSE
UniProt AC Q149C2
Protein Name TRAF3-interacting protein 1
Gene Name Traf3ip1
Organism Mus musculus (Mouse).
Sequence Length 625
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection, cilium . Cytoplasm, cytoskeleton, cilium axoneme . Cytoplasm, cytoskeleton, cilium basal body . Microtubules. In the cilium, it is observed at the ciliary base, ciliary transition zone and ciliary tip.
Protein Description Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules (By similarity). Involved in epithelial morphogenesis and in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels. [PubMed: 26487268 Involved in ciliogenesis]
Protein Sequence MNAAVVRRTQEALGKVIRRPPLTEKLLNKPPFRYLHDIITEVIRITGFMKGLYTDAEMKSENVKDKDAKISFLQKAIDVVMMVSGEPLAAKPARIVAGHEPERTNELLQLIGKCCLSKLSSDEAVKRVLAGDKGDSRGRAQRTSKAQEPNNKSGKEEESRIHKEDKRSSEAKERSASAEHKQKEELKEDSKPREKERDKEKAKEADRDRHRDPDRDRNRDGEREKARARAKDRDRNNRDRDREAERDRERDRRSEGGKEKERVKDRDRDRDKGRDRERRKSKNGEHTRDPDREKSRDADKPEKKSSSSGEISRKLSDGSFKDVKAEMEADISVGASRSSTLKPSKRRSKHSLEGDSPSDAEVEAGPAGQDKPEVMENAEVPSELPSSLRRIPRPGSARPAPPRVKRQESTETLVVDRSGSGKTVSSVIIDSQNSDNEDDEQFVVEAAPQLSEIADIDMVPSGELEDEEKHGGLVKKILETKKDYEKLQQSLKPGEKERSLIFESAWKKEKDIVSKEIEKLRVSIQTLCKSALPLGKIMDYIQEDVDAMQNELQLWHSENRQHAEALSQEQSITDSAVEPLKAELSELEQQIRDQQDKICAVKANILKNEEKIQKMVHSINLSSRR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
84PhosphorylationIDVVMMVSGEPLAAK
HCEEEECCCCCCCCC
21.3927357545
118AcetylationIGKCCLSKLSSDEAV
HHHHHHHCCCCHHHH
39.172390093
126AcetylationLSSDEAVKRVLAGDK
CCCHHHHHHHHCCCC
43.7823576753
133AcetylationKRVLAGDKGDSRGRA
HHHHCCCCCCHHHHH
64.792390109
136PhosphorylationLAGDKGDSRGRAQRT
HCCCCCCHHHHHHHC
45.3519854140
190PhosphorylationKEELKEDSKPREKER
HHHHHHCCCHHHHHH
45.7228464351
306PhosphorylationDKPEKKSSSSGEISR
CCCCCCCCCCCCHHH
37.0925338131
316PhosphorylationGEISRKLSDGSFKDV
CCHHHHHCCCCHHHH
42.8526824392
319PhosphorylationSRKLSDGSFKDVKAE
HHHHCCCCHHHHHHH
33.8322817900
351PhosphorylationSKRRSKHSLEGDSPS
CCCCCCCCCCCCCCC
31.6725293948
356PhosphorylationKHSLEGDSPSDAEVE
CCCCCCCCCCCCCCC
36.8421183079
358PhosphorylationSLEGDSPSDAEVEAG
CCCCCCCCCCCCCCC
54.1028507225
387PhosphorylationVPSELPSSLRRIPRP
CCCCCCHHHCCCCCC
24.7723140645
409PhosphorylationPRVKRQESTETLVVD
CCCCCCCCCCEEEEC
24.1725521595
410PhosphorylationRVKRQESTETLVVDR
CCCCCCCCCEEEECC
32.0327742792
412PhosphorylationKRQESTETLVVDRSG
CCCCCCCEEEECCCC
25.5827742792
614AcetylationKNEEKIQKMVHSINL
CCHHHHHHHHHHCCC
46.497624015

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MIPT3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MIPT3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MIPT3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MIPT3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MIPT3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASSSPECTROMETRY.

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